Abstract
The inhibition of yeast alcohol dehydrogenase by N′-methylnicotinamide has been shown to be due to contaminating silver ions present in commercial preparations of this reagent. Contamination by metal ions, which was assessed by quantitative analysis, also accounts for the inhibition of yeast alcohol dehydrogenase by semicarbazide. Purification of the reagents by removal of the metals abolished the inhibition. The existence of enzyme concentration-dependent inhibition serves as a kinetic indicator of such an adventitious inhibition.
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